Figure: Major histocompatibility complex class I (MHC I) peptide loading (Human)¶
This illustration depicts the Major Histocompatibility Complex class I (MHC I) peptide loading pathway in human cells. The process begins in the cytosol with peptides that are transported into the endoplasmic reticulum (ER) via the TAP1/TAP2 heterodimer transporter. Once inside the ER lumen, peptides are trimmed to the appropriate length by the aminopeptidase ERAP1. The MHC I peptide loading complex consists of the MHC I heavy chain (HLA-A) and β2-microglobulin (B2M), assisted by several chaperones: PDIA3 (protein disulfide isomerase family A member 3), TAPBP (tapasin), and CALR (calreticulin). These chaperones facilitate proper folding and assembly of the MHC I complex with the trimmed peptide. The final assembled MHC I complex with bound peptide is shown on the right side of the illustration.
Feedback from AI on figure:
{"feedback":"This illustration effectively visualizes the MHC I peptide loading pathway as described in the GO-CAM model. The drawing clearly depicts the spatial organization within the endoplasmic reticulum and the key protein interactions involved in peptide processing and loading. The color-coding system and comprehensive legend enhance understanding of this complex biological process.\n\nThe drawing accurately represents all the gene products mentioned in the GO-CAM (TAP1/TAP2, ERAP1, HLA-A, B2M, PDIA3, TAPBP, and CALR) and their functional relationships. The pathway flow is logically structured, showing peptide transport, processing, and assembly into the final MHC I complex.\n\nThe scientific accuracy is maintained while presenting the information in a visually appealing manner suitable for a high-impact journal publication.","necessary_changes":null,"optional_changes":null}